Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The interaction of human organ alkaline phosphatases (orthophosphoric-monoester phosphohydrolases (alkaline optimum), EC 3.1.3.1) with sugars was studied. Hexosamines, N-acetylneuraminic acid (NANA or sialic acid), N-acetylmuramic acid and N-acetylglycolylneuraminic acid inhibited human organ alkaline phosphatase activities. Of these, sialic acid was the most effective inhibitor. The pH profiles for the enzymes in the absence and presence of sialic acid were similar. The sialic acid - enzyme complex was more heat stable than the free enzyme between 20 and 45 degrees C. Lineweaver-Burk plots of 1/v versus 1/S at various concentrations of sialic acid showed intersecting straight lines indicating that the mechanism of inhibition was a mixed type. The Ki value obtained from the plots of 1/v versus the square of sialic acid concentration was 0.07 mM for the hepatic, sialidase-treated hepatic, and intestinal alkaline phosphatases. The respective Hill coefficients varied somewhat with the alkaline phosphatase isoenzyme. Hyperbolic curves were obtained when the percentage of remaining activity was plotted against the substrate concentration at different concentrations of sialic acid. The Hill coefficient was lowered in the presence of sialic acid. The sialidase-treated hepatic enzymes used gave the most effective conversion. Partial denaturation of the enzyme with urea, or pronase digestion had a little if any effect on the sialic acid inhibition with constant time.
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PMID:Inhibition of alkaline phosphatase by sialic acid. 1 56

A simple inexpensive method has been developed for the synthesis of [2-3H]acetophenone, which has been converted into phenyl[2-3H]glyoxal. The latter compound has been used to modify arginine residues in alkaline phosphatase from two sources, and also a sialidase.
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PMID:The synthesis of phenyl(2-3H)glyoxal. 42 78

1. Alkaline phosphatase (EC 3.1.3.1) from human liver was solubilized from the homogenate using 0.2% Triton X-100 containing 0.2 M lithium 3,5-diiodosalicylate, and the pellet obtained was resolubilized with 20% n-butanol. The procedure resulting in 3842-fold purification included acetone fractionation, ammonium sulfate precipitation, DEAE-cellulose chromatography, Sephadex G-200 gel filtration, hydroxyapatite gel chromatography and further concanavalin A/Sepharose 4B affinity chromatography. 2. The highly purified enzyme showed one major protein band on acrylamide gel electrophoresis at pH 8.6, and exhibited one-seventh of the alkaline p-nitrophenylphosphatase activity in the hepatic enzyme preparation contains of the alkaline pyrophosphatase activity. 3. The highly purified enzyme was a sialic-acid containing glycoprotein. 4. Sialidase-treated hepatic enzyme clearly presented the phenomenon of delayed mobility, and the delayed enzyme fraction stained more strongly than that of non-treated hepatic alkaline phosphatase. 5. In order to investigate the role of the carbohydrate region(s) of the hepatic alkaline phosphatase molecule on substrate binding, the effect of sialidase treatment on the rate of substrate inhibition of alkaline phosphatase was studied. In the case of hepatic enzyme without sialidase, substrate inhibition of alkaline phosphatase activity was clearly shown, while in the case of the hepatic enzyme with sialidase, there was hardly any substrate inhibition in the range of 1-8 mM p-nitrophenylphosphate.
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PMID:Partial purification and some properties of human liver alkaline phosphatase. 94 51

Asparagine-linked oligosaccharides were quantitatively released by hydrazinolysis from an alkaline phosphatase, Kasahara isozyme, which was purified from FL amnion cells. Almost all of the oligosaccharides (98%) were acidic components, all of which can be converted to neutral oligosaccharides upon sialidase digestion. Structural analysis of the oligosaccharides by sequential exoglycosidase digestion in combination with methylation analysis revealed that the alkaline phosphatase of FL cells contains sialylated mono-, bi-, tri-, and tetraantennary complex type sugar chains with the Gal beta 1----4GlcNAc beta 1---- outer chains. Some of the tetraantennary sugar chains contain a single Gal beta 1----4GlcNAc beta 1----3Gal beta 1----4GlcNAc beta 1---- outer chain on their Man alpha 1----6 arm. Both fucosylated and nonfucosylated trimannosyl cores were found in the sugar chains. However, it is of interest that the core portion of monoantennary oligosaccharide was not fucosylated and that of the tetraantennary oligosaccharide with a tetrasaccharide outer chain was completely fucosylated.
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PMID:Structures of the asparagine-linked oligosaccharides of an alkaline phosphatase, kasahara isozyme, purified from FL amnion cells. 229 56

The gross anatomy, histology and histochemistry of the ferret prostate is described. The structure and course of the prostatic urethra and the ductus deferentes are also described. The prostate is the only accessory reproductive gland present in the ferret. The prostate consists of tubuloalveolar glands surrounded by fibromuscular connective tissue. Histochemical studies showed that the glandular parenchyma contained large amounts of sialidase-labile sialomucin as well as acid phosphatase and small quantities of alkaline phosphatase and proteins. The findings in this study are discussed in relation to similar studies in other animals and man.
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PMID:Morphology and histochemistry of the ferret prostate. 242 64

We compared sialidase (neuraminidase; EC 3.2.1.18) from Vibrio cholerae, Clostridium perfringens, and Arthrobacter ureafaciens, seeking to improve the electrophoretic separation of the liver and bone isoenzymes of alkaline phosphatase (EC 3.1.3.1) on cellulose acetate membranes. Resolution is decisively determined by the type and activity of sialidase used in the preincubation of serum sample. Sialidase from Arthrobacter ureafaciens is not suited for this method. For optimal separation of the two isoenzymes we recommend the use of sialidase from Vibrio cholerae, determination of its activity with a standard procedure such as described here (mucin or sialyl lactose as substrates), and a final concentration of sialidase activity of 2.0 or 2.9 U/L (measured with mucin or sialyl lactose) in the incubation mixture.
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PMID:Sialidase from different sources compared for electrophoretically separating serum alkaline phosphatase fractions from liver and bone. 277 24

Arylsulfatase A was purified from human lung and human placenta to apparent homogeneity presented by electrophoresis in the absence and presence of sodium dodecyl sulfate. The enzyme from normal lung, placenta, and lung adenocarcinoma showed considerable charge heterogeneity when examined by isoelectrofocusing, with isoelectric point (pI) ranging from 5.1 to 4.6. The enzyme from adenocarcinoma was more heterogeneous and having more acidic components than the other enzyme. When the tumor enzyme was treated with exogenous sialidase, alkaline phosphatase, or endo-beta-N-acetylhexosaminidase H (endoglycosidase H), the acidic components of the enzyme shifted to the more alkaline region on the focussing gel. The banding pattern of the enzyme from normal tissues also changed to the more alkaline region when treated with exogenous hydrolase and showed almost the same pattern as hydrolase treated enzyme from adenocarcinoma. Combined treatment of the enzyme with endoglycosidase H and sialidase resulted in complete loss of the most acidic components to give the less acidic components with pI of 5.1.50. and 4.9. Cyclic AMP-dependent protein kinase could not phosphorylate the protein moiety of arylsulfatase A even after the enzyme was treated with alkaline phosphatase. When an acidic fraction of the endoglycosidase H sensitive oligosaccharides from arylsulfatase A was treated with phosphatase, the acidic oligosaccharide fraction lost the negative charge on QAE-Sephadex chromatography. These results strongly suggest that the charge heterogeneity of arylsulfatase A is due not only to sialylation but also to phosphorylation at the carbohydrate moiety of the enzyme, and that the extent of substitution by acidic groups, sialic acid residue and phosphate residue, is markedly increased in the tumor enzyme.
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PMID:[Studies on charge heterogeneity of arylsulfatase A from human lung cancer]. 286 24

Treatment with cholecalciferol or 1,25-dihydroxyvitamin D3 (1,25(OH)2D3) increases activity and changes electrophoretic mobility of alkaline phosphatase (alkPase) from duodenal brush border of vitamin D-deprived chicks. Three of the four molecular forms of the enzyme show reduced velocity of migration 9 h after 1,25(OH)2D3 or 24 h after vitamin D3. This change is reversed about 48 h later, when mobility of those bands is higher than that of controls. Incubation of enzyme preparations with exogenous neuraminidase produces the same electrophoretic modifications observed during the early stage, indicating that they are due to desialylation. Cholecalciferol or 1,25(OH)2D3 increase sialidase activity of duodenal brush border. This increment precedes that of alkPase and could account for the initial desialylation and moderate rise of alkPase. Cycloheximide markedly reduces alkPase in rachitic chicks and blocks the increase of the enzyme activity produced by vitamin D3, but does not modify the rise of sialidase or the reduction of alkPase electrophoretic mobility. The bimodal response of alkPase to 1,25(OH)2D3 or cholecalciferol comprises two different mechanisms: during a first stage, epigenetic modifications of preexisting enzyme can be triggered by the increased Ca2+ levels; in a second phase, there is activation of enzyme synthesis.
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PMID:Changes of intestinal alkaline phosphatase produced by cholecalciferol or 1,25-dihydroxyvitamin D3 in vitamin D-deficient chicks. 299 Mar 44

Gastric and intestinal phenotypic expression in 37 surgically obtained primary signet ring cell carcinomas, five of their metastases to lymph nodes, and three signet ring cell carcinomas transplanted into nude mice were determined by biochemical, mucin, histochemical, and ultrastructural studies. Crude extracts of cancer tissues were used for measurements of pepsinogen isozymes, sucrase, aminopeptidase (microsomal), and alkaline phosphatase. Histochemical staining of mucin by paradoxical concanavalin A, the galactose oxidase-Schiff sequence and sialidase-galactose oxidase-Schiff, and the periodate-borohydride technique/potassium hydroxide/periodic acid-Schiff procedure was performed. The procedures allowed clear definition of pyloric gland, surface mucous, small and large intestinal goblet, and intestinal absorptive cell types. Of 40 specimens examined, 19 consisted entirely of gastric-type cells, and three entirely of intestinal-type cells. The others consisted of mixtures of gastric and intestinal-type cells. The observed high incidence of intestinal-type cells in signet ring cell carcinomas suggested that intestinal-type cells develop independently from intestinal metaplasia within signet ring cell carcinomas (diffuse-type gastric cancers), which probably originate from nonmetaplastic gastric mucosa.
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PMID:Gastric and intestinal phenotypic expressions of human signet ring cell carcinomas revealed by their biochemistry, mucin histochemistry, and ultrastructure. 301

Isoenzymes of alkaline phosphatase (EC 3.1.3.1) were separated by micro-scale two-dimensional electrophoresis, with isoelectric focusing in capillary gels in the first dimension and polyacrylamide gradient-gel electrophoresis in the second. The isoenzymes detected were identified by several treatments--e.g., incubation with sialidase, papain, Triton X-100, and wheat-germ agglutinin--and by comparison with alkaline phosphatase from liver microsomes. Liver and bone isoforms in normal sera showed overlapping isoelectric points but differed in molecular mass, estimated as 172 and 185 kDa, respectively. Sera of patients with liver disease showed several additional groups of alkaline phosphatase isoforms, two of which were found to consist of multi-molecular complexes. Others probably correspond to incompletely glycated enzyme proteins. A further isoform with a mass of about 250 kDa does not seem to correspond to any known isoform of alkaline phosphatase in serum. With this technique, we demonstrated intra- and interindividual variations of the placental alkaline phosphatase isoenzyme in pregnancy sera.
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PMID:Micro-scale two-dimensional electrophoresis of alkaline phosphatase from serum. 335 9


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